Monolayers assembled from a glycolipid biosurfactant from Pseudozyma (Candida) antarctica serve as a high-affinity ligand system for immunoglobulin G and M

被引：34
作者：
Imura, Tomohiro
Ito, Seya
Azumi, Reiko
Yanagishita, Hiroshi
Sakai, Hideki
Abe, Masahiko
Kitamoto, Dai
机构：
[1] Natl Inst Adv Ind Sci & Technol, Res Inst Innovat Sustainable Chem, Tsukuba, Ibaraki 3058565, Japan
[2] Tokyo Univ Sci, Fac Sci & Technol, Noda, Chiba 2788510, Japan
[3] Natl Inst Adv Ind Sci & Technol, Photon Res Inst, Tsukuba, Ibaraki 3058565, Japan
来源：
BIOTECHNOLOGY LETTERS | 2007年 / 29卷 / 06期
关键词：
atomic force microscopy; biosurfactant; immunoglobulin; protein-carbohydrate interaction; surface plasmon resonance;
D O I：
10.1007/s10529-007-9335-4
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
A carbohydrate ligand system has been developed which is composed of self-assembled monolayers (SAMs) of mannosylerythritol lipid-A (MEL-A) from Pseudozyma antarctica, serving for human immunoglobulin G and M (HIgG and HIgM). The estimated binding constants from surface plasmon resonance (SPR) measurement were K-a = 9.4 x 10(6) M-1 for HIgG and 5.4 x 10(6) M-1 for HIgM, respectively. The binding site was not in the Fc region of immunoglobulin but in the Fab region. Large amounts of HIgG and HIgM bound to MEL-A SAMs were directly observed by atomic force microscopy.
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页码：865 / 870
页数：6
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